UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1

Sunghoi Hong, Soyeon Lee, Ssang Goo Cho, Seongman Kang

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

UbcH6 is a member of an evolutionally conserved subfamily of E2 ubiquitin-conjugating enzymes. In this study, we report that UbcH6 interacts with and ubiquitinates ataxin-1, the spinocerebellar ataxia type 1 gene product. UbcH6 was identified as an ataxin-1-interacting protein using a yeast two-hybrid screen. UbcH6 co-immunoprecipitates and co-localizes with the ataxin-1 protein in the nucleus. Our binding assays showed that ataxin-1 interacts with UbcH6 through its AXH domain. Interestingly, UbcH6 could ubiquitinate ataxin-1 in the absence of an E3 ligase. The expression level of UbcH6 regulated the rate of ataxin-1 degradation. This study demonstrates that UbcH6 and ataxin-1 are E2-substrate cognate pairs in the ubiquitin-proteasome system.

Original languageEnglish
Pages (from-to)256-260
Number of pages5
JournalBiochemical and biophysical research communications
Volume371
Issue number2
DOIs
Publication statusPublished - 2008 Jun 27

Keywords

  • AXH domain
  • Ataxin-1
  • UbcH6
  • Ubiquitination

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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